Here, we characterized the structure of the two-component regulatory system, LisR/LisK, in Listeria monocytogenes. To predict the structure of both proteins and the relationship between them, we employed several bioinformatic tools and databases. Based on our results, LisK protein is embedded in the...

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Autores:
Arenas Suarez, Nelson; Department of Biochemistry and Molecular Biology. University of Southern Denmark campusvej 55. 5230 Odense M, Denmark
Gutiérrez Escobar, Andrés; Grupo de Investigación GIBGA. Facultad de Medicina. Universidad de Ciencias Aplicadas y Ambientales. U.D.C.A.
Sánchez-Goméz, Myriam; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Salazar, Luz Mary; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Reyes Montaño, Edgar; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Tipo de recurso:
Article of journal
Fecha de publicación:
2013
Institución:
Pontificia Universidad Javeriana
Repositorio:
Repositorio Universidad Javeriana
Idioma:
eng
OAI Identifier:
oai:repository.javeriana.edu.co:10554/32009
Acceso en línea:
http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757
http://hdl.handle.net/10554/32009
Palabra clave:
Bioinformatics and Modeling
Listeria monocytogenes ; LisR/LisK; two-component regulatory systems; protein histidine kinase.
Proteínas
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openAccess
License
Atribución-NoComercial-SinDerivadas 4.0 Internacional
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repository_id_str
spelling Atribución-NoComercial-SinDerivadas 4.0 Internacionalinfo:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2nullArenas Suarez, Nelson; Department of Biochemistry and Molecular Biology. University of Southern Denmark campusvej 55. 5230 Odense M, DenmarkGutiérrez Escobar, Andrés; Grupo de Investigación GIBGA. Facultad de Medicina. Universidad de Ciencias Aplicadas y Ambientales. U.D.C.A.Sánchez-Goméz, Myriam; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.Salazar, Luz Mary; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.Reyes Montaño, Edgar; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.2018-02-24T16:01:11Z2020-04-15T18:09:02Z2018-02-24T16:01:11Z2020-04-15T18:09:02Z2013-08-26http://revistas.javeriana.edu.co/index.php/scientarium/article/view/475710.11144/Javeriana.SC18-2.sfts2027-13520122-7483http://hdl.handle.net/10554/32009PDFapplication/pdfapplication/pdftext/htmlengPontificia Universidad Javerianahttp://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757/4914http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757/4915http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757/6502Universitas Scientiarum; Vol 18, No 2 (2013); 189-202Universitas Scientiarum; Vol 18, No 2 (2013); 189-202Universitas Scientiarum; Vol 18, No 2 (2013); 189-202Bioinformatics and ModelingListeria monocytogenes ; LisR/LisK; two-component regulatory systems; protein histidine kinase.Proteínasnullnullnullhttp://purl.org/coar/version/c_970fb48d4fbd8a85Artículo de revistahttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/articleStructural features of the two-component system LisR/LisK suggests multiple responses for the adaptation and survival of Listeria monocytogenesHere, we characterized the structure of the two-component regulatory system, LisR/LisK, in Listeria monocytogenes. To predict the structure of both proteins and the relationship between them, we employed several bioinformatic tools and databases. Based on our results, LisK protein is embedded in the cell membrane and its modular composition (HAMP, histidine kinase and ATPase domains) is associated with its autophosphorylation (His-266). A stimulus-response likely determines the sequential signal propagation from the bacterial cell surface to its cytoplasmic components. According to our results, LisR is a cytoplasmic protein with a receptor domain (homologous to CheY) that comprises a phosphoacceptor residue (Asp-52) and a DNA-binding domain, which may allow the transmission of a specific transcriptional response. LisR/LisK has been experimentally characterized both biochemically and functionally in other Bacilli pathophysiology; our structure-function approach may facilitate the design of suitable inhibitors.10554/32009oai:repository.javeriana.edu.co:10554/320092023-03-28 16:14:56.08Repositorio Institucional - Pontificia Universidad Javerianarepositorio@javeriana.edu.co
dc.title.english.eng.fl_str_mv Structural features of the two-component system LisR/LisK suggests multiple responses for the adaptation and survival of Listeria monocytogenes
dc.creator.fl_str_mv Arenas Suarez, Nelson; Department of Biochemistry and Molecular Biology. University of Southern Denmark campusvej 55. 5230 Odense M, Denmark
Gutiérrez Escobar, Andrés; Grupo de Investigación GIBGA. Facultad de Medicina. Universidad de Ciencias Aplicadas y Ambientales. U.D.C.A.
Sánchez-Goméz, Myriam; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Salazar, Luz Mary; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Reyes Montaño, Edgar; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
dc.contributor.author.none.fl_str_mv Arenas Suarez, Nelson; Department of Biochemistry and Molecular Biology. University of Southern Denmark campusvej 55. 5230 Odense M, Denmark
Gutiérrez Escobar, Andrés; Grupo de Investigación GIBGA. Facultad de Medicina. Universidad de Ciencias Aplicadas y Ambientales. U.D.C.A.
Sánchez-Goméz, Myriam; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Salazar, Luz Mary; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
Reyes Montaño, Edgar; Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá. Colombia.
dc.contributor.none.fl_str_mv null
dc.subject.eng.fl_str_mv Bioinformatics and Modeling
Listeria monocytogenes ; LisR/LisK; two-component regulatory systems; protein histidine kinase.
Proteínas
topic Bioinformatics and Modeling
Listeria monocytogenes ; LisR/LisK; two-component regulatory systems; protein histidine kinase.
Proteínas
spellingShingle Bioinformatics and Modeling
Listeria monocytogenes ; LisR/LisK; two-component regulatory systems; protein histidine kinase.
Proteínas
description Here, we characterized the structure of the two-component regulatory system, LisR/LisK, in Listeria monocytogenes. To predict the structure of both proteins and the relationship between them, we employed several bioinformatic tools and databases. Based on our results, LisK protein is embedded in the cell membrane and its modular composition (HAMP, histidine kinase and ATPase domains) is associated with its autophosphorylation (His-266). A stimulus-response likely determines the sequential signal propagation from the bacterial cell surface to its cytoplasmic components. According to our results, LisR is a cytoplasmic protein with a receptor domain (homologous to CheY) that comprises a phosphoacceptor residue (Asp-52) and a DNA-binding domain, which may allow the transmission of a specific transcriptional response. LisR/LisK has been experimentally characterized both biochemically and functionally in other Bacilli pathophysiology; our structure-function approach may facilitate the design of suitable inhibitors.
publishDate 2013
dc.date.created.none.fl_str_mv 2013-08-26
dc.date.accessioned.none.fl_str_mv 2018-02-24T16:01:11Z
2020-04-15T18:09:02Z
dc.date.available.none.fl_str_mv 2018-02-24T16:01:11Z
2020-04-15T18:09:02Z
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_2df8fbb1
dc.type.hasversion.none.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.local.spa.fl_str_mv Artículo de revista
dc.type.coar.none.fl_str_mv http://purl.org/coar/resource_type/c_6501
dc.type.driver.none.fl_str_mv info:eu-repo/semantics/article
format http://purl.org/coar/resource_type/c_6501
dc.identifier.none.fl_str_mv http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757
10.11144/Javeriana.SC18-2.sfts
dc.identifier.issn.none.fl_str_mv 2027-1352
0122-7483
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/10554/32009
url http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757
http://hdl.handle.net/10554/32009
identifier_str_mv 10.11144/Javeriana.SC18-2.sfts
2027-1352
0122-7483
dc.language.iso.none.fl_str_mv eng
language eng
dc.relation.uri.none.fl_str_mv http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757/4914
http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757/4915
http://revistas.javeriana.edu.co/index.php/scientarium/article/view/4757/6502
dc.relation.citationissue.eng.fl_str_mv Universitas Scientiarum; Vol 18, No 2 (2013); 189-202
dc.relation.citationissue.spa.fl_str_mv Universitas Scientiarum; Vol 18, No 2 (2013); 189-202
dc.relation.citationissue.por.fl_str_mv Universitas Scientiarum; Vol 18, No 2 (2013); 189-202
dc.rights.licence.*.fl_str_mv Atribución-NoComercial-SinDerivadas 4.0 Internacional
dc.rights.accessrights.none.fl_str_mv info:eu-repo/semantics/openAccess
dc.rights.coar.spa.fl_str_mv http://purl.org/coar/access_right/c_abf2
rights_invalid_str_mv Atribución-NoComercial-SinDerivadas 4.0 Internacional
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.spa.fl_str_mv PDF
dc.format.mimetype.spa.fl_str_mv application/pdf
application/pdf
text/html
dc.coverage.none.fl_str_mv null
null
null
dc.publisher.eng.fl_str_mv Pontificia Universidad Javeriana
institution Pontificia Universidad Javeriana
repository.name.fl_str_mv Repositorio Institucional - Pontificia Universidad Javeriana
repository.mail.fl_str_mv repositorio@javeriana.edu.co
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